ArticleVirology2007
The role of lysine 186 in HIV-1 integrase multimerization.
Article in Virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 38 citations in OpenAlex.
- Conjugated Polymers Based on Carbazole and Tridentate Ligands as the "On-Off-On" Fluorescent Probes for Detection of Ni (II) Ion and Lysine.Journal of fluorescence · 2025Article
- Molecular dissection of an inhibitor targeting the HIV integrase dependent preintegration complex nuclear import.Cellular microbiology · 2019Article
- Critical Contribution of Tyr15 in the HIV-1 Integrase (IN) in Facilitating IN Assembly and Nonenzymatic Function through the IN Precursor Form with Reverse Transcriptase.Journal of virology · 2017Article
- The Preserved HTH-Docking Cleft of HIV-1 Integrase Is Functionally Critical.Structure (London, England : 1993) · 2016Article
- Human immunodeficiency virus type 1 employs the cellular dynein light chain 1 protein for reverse transcription through interaction with its integrase protein.Journal of virology · 2015Article
- Uneven genetic robustness of HIV-1 integrase.Journal of virology · 2015Article
- Dual inhibition of HIV-1 replication by integrase-LEDGF allosteric inhibitors is predominant at the post-integration stage.Retrovirology · 2013Article
- A doubly fluorescent HIV-1 reporter shows that the majority of integrated HIV-1 is latent shortly after infection.Journal of virology · 2013Article
- Correlation of recombinant integrase activity and functional preintegration complex formation during acute infection by replication-defective integrase mutant human immunodeficiency virus.Journal of virology · 2012Article
- Inhibition of HIV-1 infection by TNPO3 depletion is determined by capsid and detectable after viral cDNA enters the nucleus.Retrovirology · 2011Article
- Review
- Host protein Ku70 binds and protects HIV-1 integrase from proteasomal degradation and is required for HIV replication.The Journal of biological chemistry · 2011Article
- Structural biology of retroviral DNA integration.Virology · 2011Review
- Structural properties of HIV integrase. Lens epithelium-derived growth factor oligomers.The Journal of biological chemistry · 2010Article
- Crystal structures of catalytic core domain of BIV integrase: implications for the interaction between integrase and target DNA.Protein & cell · 2010Article
- Characterization of the HIV-1 integrase chromatin- and LEDGF/p75-binding abilities by mutagenic analysis within the catalytic core domain of integrase.Virology journal · 2010Article
- The Interaction Between Lentiviral Integrase and LEDGF: Structural and Functional Insights.Viruses · 2009Article
- Article
- Structural basis for functional tetramerization of lentiviral integrase.PLoS pathogens · 2009Article
- Contribution of the C-terminal region within the catalytic core domain of HIV-1 integrase to yeast lethality, chromatin binding and viral replication.Retrovirology · 2008Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
HIV-1 integrase (IN) catalyzes biochemical reactions required for viral cDNA insertion into host cell chromosomal DNA, an essential step in the HIV-1 replication cycle. In one of these reactions, the two ends of the linear viral cDNA are believed to be simultaneously ligated to chromosomal DNA by a tetrameric form of IN. The structure of the full-length IN tetramer is not known but a model consisting of the N-terminal domain and the catalytic core revealed basic residues 186 to 188 at the interface between the two IN dimers. We found that alteration of these residues, in particular changing IN lysine residue 186 to glutamate (K186Q), impairs IN oligomerization in the yeast two-hybrid system and decreases oligomeric forms of IN within virions. When expressed independently of other viral proteins in human cells, IN-K186Q did not concentrate in the nucleus as did wild-type IN. Co-expression of wild-type IN restored the multimerization defects of IN-K186Q, in both the two-hybrid system and in virions, and also rescued the nuclear targeting defects. Virions bearing IN-K186Q were not infectious in a single cycle of replication but when mixed virions containing two different IN mutants were produced, IN-K186Q was capable of complementing the catalytically inactive mutant IN-D116A. Our biochemical and functional data support the crystallographic model in which IN residue K186 lies at the interface between IN dimers and suggest that tetramerization is important, not only for concerted integration, but also for IN nuclear targeting.
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